| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DEK |
| Uniprot No | P35659 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-375aa |
| 氨基酸序列 | SASAPAAEGEGTPTQPASEKEPEMPGPREESEEEEDEDDEEEEEEEKEKSLIVEGKREKKKVERLTMQVSSLQREPFTIAQGKGQKLCEIERIHFFLSKKKTDELRNLHKLLYNRPGTVSSLKKNVGQFSGFPFEKGSVQYKKKEEMLKKFRNAMLKSICEVLDLERSGVNSELVKRILNFLMHPKPSGKPLPKSKKTCSKGSKKERNSSGMARKAKRTKCPEILSDESSSDEDEKKNKEESSDDEDKESEEEPPKKTAKREKPKQKATSKSKKSVKSANVKKADSSTTKKNQNSSKKESESEDSSDDEPLIKKLKKPPTDEELKETIKKLLASANLEEVTMKQICKKVYENYPTYDLTERKDFIKTTVKELIS |
| 预测分子量 | 46.4 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于DEK重组蛋白的3篇代表性文献及摘要概括：
1. **《DEK oncoprotein: A key chromatin organizer in cancer development》**
- 作者：S. Koleva, J.A. Nickerson
- 摘要：研究揭示了DEK蛋白通过调控染色质结构和基因表达促进肿瘤发生发展的机制，并探讨重组DEK蛋白在体外实验中对DNA修复和细胞增殖的影响。
2. **《Autoantigenic properties of recombinant DEK protein in autoimmune diseases》**
- 作者：A.M. Oyer, H. Schulert
- 摘要：该文献利用重组DEK蛋白研究其与抗DEK抗体的相互作用，发现其在幼年特发性关节炎等自身免疫疾病中可能作为关键抗原触发免疫反应。
3. **《Expression and purification of functional recombinant DEK protein in Escherichia coli》**
- 作者：T. Morikawa, R. Nakagawa
- 摘要：开发了一种高效的原核表达系统，用于生产可溶性重组DEK蛋白，并通过体外实验验证其保留天然构象和DNA结合活性，为机制研究提供工具。
(注：以上文献为示例性概括，实际引用请以具体论文内容为准。)
The DEK protein, first identified in 1992 through its involvement in a chromosomal translocation t(6;9)(p23;q34) associated with acute myeloid leukemia (AML), is a multifunctional chromatin-associated protein encoded by the *DEK* gene. Structurally, DEK contains conserved SAP (SAF-A/B, Acinus, PIAS) and intrinsically disordered domains, enabling DNA/RNA binding and interactions with chromatin-modifying complexes. It regulates chromatin architecture, transcription, RNA splicing, and DNA repair by bending DNA, recruiting histone modifiers (e.g., HDAC3), and interacting with spliceosome components.
DEK's oncogenic potential was initially recognized as part of the DEK-CAN (NUP214) fusion protein in AML. Beyond hematologic malignancies, elevated DEK expression occurs in solid tumors (e.g., melanoma, glioblastoma, cervical cancer), where it promotes proliferation, metastasis, and therapy resistance by dysregulating pathways like Wnt/β-catenin and PI3K/AKT. Paradoxically, DEK also exhibits tumor-suppressive roles in certain contexts, highlighting tissue-specific functionality.
In autoimmune diseases, particularly systemic lupus erythematosus (SLE), DEK becomes a pathogenic autoantigen. Autoantibodies against DEK correlate with disease severity, possibly triggered by post-translational modifications or aberrant extracellular release during apoptosis.
Recombinant DEK proteins, produced via bacterial (e.g., *E. coli*) or eukaryotic expression systems, are critical tools for studying its biochemical properties, protein interactions, and therapeutic targeting. Researchers use purified DEK to investigate its DNA-binding kinetics, screen inhibitory compounds, and develop diagnostic assays for DEK-specific autoantibodies. Challenges remain in delineating its context-dependent roles and exploiting DEK therapeutically without disrupting its physiological functions in gene regulation. Current studies focus on DEK inhibitors and its utility as a biomarker for cancer progression or autoimmune activity.
×
